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1997 Fiscal Year Final Research Report Summary

TYPE III EXPORT SYSTEM ; STRUCTURAL ANALYSIS OF FLAGELLA-SPECIFIC EXPORT APPARATUS OF BACTERIA

Research Project

Project/Area Number 08458222
Research Category

Grant-in-Aid for Scientific Research (B)

Allocation TypeSingle-year Grants
Section一般
Research Field Molecular biology
Research InstitutionTEIKYO UNIVERSITY

Principal Investigator

AIZAWA Shin-ichi  TEIKYO UNIVERSITY,BIOSCIENCES,ASSOCIATE PROFESSOR, 理工学部, 助教授 (50222451)

Co-Investigator(Kenkyū-buntansha) KATAYAMA Eisaku  THE UNIVERSITY OF TOKYO,INSTITUTE OF MEDICAL SCIENCE,ASSOCIATE PROFESSOR, 医科学研究所, 助教授 (50111505)
Project Period (FY) 1996 – 1997
KeywordsBACTERIA / FLAGELLA / EXPORT APPARATUS / PATHOGENICITY / TYPE III EXPORT SYSTEMS
Research Abstract

Bacterial flagellum is an extracellular organelle. Therefore, most of the component proteins once synthesized in the cytoplasm have to be exported outside the cell through an export apparatus specific for flagellar proteins.
Among the component proteins in the apparatus, FliH and FliI proteins are regarded to work as a gate keeper, because the deletion mutants of those genes result in blockage of flagellation at the early steps.
We have developed a method to visualize flagellar basal structures from inside the cell. The method includes revised techniques for preparing osmotically-shocked cells, and the quick-freeze deep-ethch electron microscopy. We have succeeded in visualization of the flagellar C ring structure of Salmonella typhimurium.
Furthermore, in the course of developing the methods, we found a supramolecular structure resembling to flagellar basal body. Since it has a straight needle instead of the curved hook, we call the structure the needle complex. The needle complexes were purified, separated into components by SDS-PAGE, blotted onto nitrocellulose papers, and analyzed by the amino acid sequencer. The major component proteins were identified as PrgH, PrgK, and InvG that are known as pathogenic factors. These results strongly support a hypothesis that flagella and pathogenicity have the same origin.

  • Research Products

    (17 results)

All Other

All Publications (17 results)

  • [Publications] Kubori et al: "The invasion-associated type III protein secretion system forms a supramolecular structure・・・・" Science. 280. 602-605 (1998)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Saito et.al.: "Flagellar filament elongation can be impaired by mutations in the hook protein FlgE" Mol.Microbiol.27. 1129-1140 (1998)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Muramoto et.al.: "Effect of cellular level of Flik on flagellar hook" J.Mol.Biol.277. 871-882 (1998)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Koroyasu et al.: "Kinetic analysis of the growth rate of the flagellar hook" Biophysical J.74. 436-443 (1998)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Kubori et.al: "Assembly of the switch complex outo the MS ring complex" J.Bacteriol. 179. 813-817 (1997)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] Aizawa: "Flagellar Assembly in Salmonella typhjmunum." Mol.Microbiol.19. 1-5 (1996)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] 相沢慎一: "バクテリアのべん毛モーター" 共立出版, 142 (1998)

    • Description
      「研究成果報告書概要(和文)」より
  • [Publications] S.-I.Aizawa: "Flagellar Assembly in Salmonella typhimurium" Mol.Microbiol. 19. 1-5 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] E.Katayama, T.Shiraishi, K.Oosawa, N.Baba, & S.-I.Aizawa: "Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images" J.Mol.Biol.255. 458-475 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] A.W.Williams, S.Yamaguchi, F.Togashi, S.-I.Aizawa, I.Kawagishi, & R.M.Macnab: "Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium" J.Bacteriol. 178. 2960-2970 (1996)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kubori, T., Yamaguchi, S., & Aizawa, S.-I.: "Assembly of the Switch Complex onto the MS Ring Complex of Salmonella typhimurium Does Not Require Any Other Flagellar Proteins" J.Bacteriol.179. 813-817 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Togashi, F., Yamaguchi, S., Kihara, M., Aizawa, S.-I., & Macnab, R.M.: "An Extreme Clockwise Switch Bias Mutation in FliG of Salmonella and Its Suppression by Slow-Motile Mutations in motA and motB" J.Bacteriol. 179. 2994-3003 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kubori, T., Okumura, M., Kobayashi, N., Nakamura, D., Iwakura, M., & Aizawa, S.-I.: "Purification and characterization of the flagellar hook-basal body complex of Bacillus subtilis" Mol.Microbiol.24. 399-410 (1997)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Koroyasu, S., Yamazato, M., Hirano, T., & Aizawa, S.-I.: "Kinetic analysis of the growth rate of the flagellar hook in Salmonella typhimurium by the population balance method" Biophysical J.74. 436-443 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Muramoto, K., Makishima, S., Aizawa, S.-I., and Macnab, R.M.: "Effect of cellular level of FliK on flagellar hook and filament assembly in Salmonella typhimurium" J.Mol.Biol.277. 871-882 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Saito, T., Ueno, T., Kubori, T., Yamaguchi, S., Iino, T., & Aizawa, S.-I.: "Flagellar filament elongation can be impaired by mutations in the hook protein FlgE of Salmonella typhimurium ; A possible role of the hook as a passage for the anti-sigma factor FlgM" Mol.Microbiol.27. 1129-1140 (1998)

    • Description
      「研究成果報告書概要(欧文)」より
  • [Publications] Kubori, T., et al.: "The invasion-associated type III protein secretion system forms a supramolecular structure on envelope of Salmonella typhimurium" Science. 280. 602-605 (1998)

    • Description
      「研究成果報告書概要(欧文)」より

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Published: 1999-12-08  

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